PDB-1ss8: GroEL - Yorodumi

ID or keywords:

Entry

Database: PDB / ID: 1ss8

Title

GroEL

Components

groEL protein

Keywords

CHAPERONE / chaperonin / protein folding

Function / homology

Function and homology information

GroEL-GroES complex / chaperonin ATPase / virion assembly / ATP-dependent protein folding chaperone / response to radiation / protein refolding / response to heat / protein folding / magnesium ion binding / ATP hydrolysis activity ...
Similarity search - Function

Biological species

Escherichia coli (E. coli)

Method

X-RAY DIFFRACTION /

FOURIER SYNTHESIS / Resolution: 2.7 Å

Authors

Chaudhry, C. / Horwich, A.L. / Brunger, A.T. / Adams, P.D.

Citation

Journal: J.Mol.Biol. / Year: 2004
Title: Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states.
Authors: Chaudhry, C. / Horwich, A.L. / Brunger, A.T. / Adams, P.D.

History

Deposition	Mar 23, 2004	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Mar 1, 2005	Provider: repository / Type: Initial release
Revision 1.1	Apr 29, 2008	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Advisory / Derived calculations / Version format compliance
Revision 1.3	Mar 26, 2014	Group: Other
Revision 1.4	Oct 11, 2017	Group: Refinement description / Category: software
Revision 1.5	Feb 14, 2024	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.end_auth_comp_id

Remark 999

SEQUENCE THE CONFLICTS ARE PRESENT IN RELATED ENTRY 1OEL.

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

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Others	Other downloads

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/ss/1ss8 ftp://data.pdbj.org/pub/pdb/validation_reports/ss/1ss8	HTTPS FTP

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Related structure data

Related structure data	1svtC 1sx3C 1sx4C 1oel C: citing same article (ref.)
Similar structure data	1oel-1 2nwc-d 1sx3-d 1xck-d 4hel-d 1kp8-d 2ynj-d 6kfv-d 4v43-2 4wgl-d 5w0s-d 4wsc-d 5opw-d 2yey-d Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#32 - Aug 2002 Chaperones similarity (11)

Deposited unit

A: groEL protein

B: groEL protein

C: groEL protein

D: groEL protein

E: groEL protein

F: groEL protein

G: groEL protein

386 kDa, 7 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: groEL protein

B: groEL protein

C: groEL protein

D: groEL protein

E: groEL protein

F: groEL protein

G: groEL protein

A: groEL protein

B: groEL protein

C: groEL protein

D: groEL protein

E: groEL protein

F: groEL protein

G: groEL protein

defined by author&software
772 kDa, 14 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

Idetical with deposited unit
defined by software

Unit cell

Length a, b, c (Å)	178.380, 204.980, 280.980
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	20
Space group name H-M	C222₁

Noncrystallographic symmetry (NCS)

NCS domain:
NCS domain segments:

Refine code: 1

Dom-ID	Component-ID	Ens-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	1	ALA	ALA	SER	SER	A	A	2 - 135	1 - 134
2	1	1	ALA	ALA	SER	SER	B	B	2 - 135	1 - 134
3	1	1	ALA	ALA	SER	SER	C	C	2 - 135	1 - 134
4	1	1	ALA	ALA	SER	SER	D	D	2 - 135	1 - 134
5	1	1	ALA	ALA	SER	SER	E	E	2 - 135	1 - 134
6	1	1	ALA	ALA	SER	SER	F	F	2 - 135	1 - 134
7	1	1	ALA	ALA	SER	SER	G	G	2 - 135	1 - 134
8	2	1	GLY	GLY	PRO	PRO	A	A	410 - 525	409 - 524
9	2	1	GLY	GLY	PRO	PRO	B	B	410 - 525	409 - 524
10	2	1	GLY	GLY	PRO	PRO	C	C	410 - 525	409 - 524
11	2	1	GLY	GLY	PRO	PRO	D	D	410 - 525	409 - 524
12	2	1	GLY	GLY	PRO	PRO	E	E	410 - 525	409 - 524
13	2	1	GLY	GLY	PRO	PRO	F	F	410 - 525	409 - 524
14	2	1	GLY	GLY	PRO	PRO	G	G	410 - 525	409 - 524
1	1	2	VAL	VAL	VAL	VAL	A	A	136 - 190	135 - 189
2	1	2	VAL	VAL	VAL	VAL	B	B	136 - 190	135 - 189
3	1	2	VAL	VAL	VAL	VAL	C	C	136 - 190	135 - 189
4	1	2	VAL	VAL	VAL	VAL	D	D	136 - 190	135 - 189
5	1	2	VAL	VAL	VAL	VAL	E	E	136 - 190	135 - 189
6	1	2	VAL	VAL	VAL	VAL	F	F	136 - 190	135 - 189
7	1	2	VAL	VAL	VAL	VAL	G	G	136 - 190	135 - 189
8	2	2	GLY	GLY	GLU	GLU	A	A	375 - 409	374 - 408
9	2	2	GLY	GLY	GLU	GLU	B	B	375 - 409	374 - 408
10	2	2	GLY	GLY	GLU	GLU	C	C	375 - 409	374 - 408
11	2	2	GLY	GLY	GLU	GLU	D	D	375 - 409	374 - 408
12	2	2	GLY	GLY	GLU	GLU	E	E	375 - 409	374 - 408
13	2	2	GLY	GLY	GLU	GLU	F	F	375 - 409	374 - 408
14	2	2	GLY	GLY	GLU	GLU	G	G	375 - 409	374 - 408
1	1	3	GLU	GLU	GLY	GLY	A	A	191 - 374	190 - 373
2	1	3	GLU	GLU	GLY	GLY	B	B	191 - 374	190 - 373
3	1	3	GLU	GLU	GLY	GLY	C	C	191 - 374	190 - 373
4	1	3	GLU	GLU	GLY	GLY	D	D	191 - 374	190 - 373
5	1	3	GLU	GLU	GLY	GLY	E	E	191 - 374	190 - 373
6	1	3	GLU	GLU	GLY	GLY	F	F	191 - 374	190 - 373
7	1	3	GLU	GLU	GLY	GLY	G	G	191 - 374	190 - 373

NCS ensembles :

ID
1
2
3

Details

THE COMPLETE GROEL COMPLEX (2 BACK-TO-BACK RINGS) IS GENERATED BY THE APPLICATION OF THE SYMMETRY OPERATOR (X,-Y,-Z) TO THE 7 PROTOMERS IN THE ASYMMETRIC UNIT.

#1: Protein	groEL protein / Protein Cpn60 / 60 kDa chaperonin Mass: 55148.020 Da / Num. of mol.: 7 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) Gene: GROL, GROEL, MOPA, B4143, C5227, Z5748, ECS5124, SF4297, S4564 Plasmid: trc / Production host: Escherichia coli (E. coli) / Strain (production host): DH5a / References: UniProt: P0A6F5
#2: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 107 / Source method: isolated from a natural source / Formula: H₂O

#1: Protein

groEL protein / Protein Cpn60 / 60 kDa chaperonin

Mass: 55148.020 Da / Num. of mol.: 7
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Escherichia coli (E. coli)
Gene: GROL, GROEL, MOPA, B4143, C5227, Z5748, ECS5124, SF4297, S4564
Plasmid: trc / Production host:

Escherichia coli (E. coli) / Strain (production host): DH5a / References: UniProt: P0A6F5

#2: Water

ChemComp-HOH / water

Mass: 18.015 Da / Num. of mol.: 107 / Source method: isolated from a natural source / Formula: H₂O

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Experiment

Experiment	Method: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

Crystal	Density Matthews: 3.33 Å³/Da / Density % sol: 63.03 %
Crystal grow	Temperature: 298 K / Method: evaporation, recrystallization / pH: 8 Details: PEG 8000, 1.72 M ammonium slufate, 4 mM CaCl2, 100mM Tris-acetate , pH 8.0, EVAPORATION, RECRYSTALLIZATION, temperature 298K

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Data collection

Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Relative weight: 1
Reflection	Resolution: 2.7→30.015 Å / Num. all: 123506 / Num. obs: 117825 / Limit h max: 60 / Limit h min: 0 / Limit k max: 75 / Limit k min: 0 / Limit l max: 100 / Limit l min: 0

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Processing

Software

Name	Version	Classification
REFMAC	refmac_5.1.19	refinement
DENZO		data reduction
SCALEPACK		data scaling
MLPHARE		phasing

Refinement

Method to determine structure:

FOURIER SYNTHESIS / Resolution: 2.7→30 Å / Cor.coef. F_o:F_c: 0.914 / Cor.coef. F_o:F_c free: 0.89 / SU B: 14.259 / SU ML: 0.279 / SU R Cruickshank DPI: 1.208 / TLS residual ADP flag: LIKELY RESIDUAL / σ(F): 0 / ESU R: 1.208 / ESU R Free: 0.334 / Stereochemistry target values: Engh & Huber

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.249	2966	2.517 %	RANDOM
R_work	0.215	-	-	-
all	0.216	117825	-	-
obs	0.216	117825	-	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL PLUS MASK

Displacement parameters

B_iso mean: 2.604 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-1.211 Å²	0 Å²	0 Å²
2-	-	-1.539 Å²	0 Å²
3-	-	-	2.75 Å²

Refinement step

Cycle: LAST / Resolution: 2.7→30 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	26957	0	0	107	27064

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.027	0.022	27153
X-RAY DIFFRACTION	r_angle_refined_deg	2.043	1.984	36666
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.881	5	3661
X-RAY DIFFRACTION	r_chiral_restr	0.134	0.2	4466
X-RAY DIFFRACTION	r_gen_planes_refined	0.007	0.02	19740
X-RAY DIFFRACTION	r_xyhbond_nbd_refined	0.175	0.2	652
X-RAY DIFFRACTION	r_symmetry_vdw_refined	0.422	0.2	98
X-RAY DIFFRACTION	r_symmetry_hbond_refined	0.367	0.2	5
X-RAY DIFFRACTION	r_mcbond_it	0.297	1.5	18081
X-RAY DIFFRACTION	r_mcangle_it	0.489	2	28938
X-RAY DIFFRACTION	r_scbond_it	1.137	3	9072
X-RAY DIFFRACTION	r_scangle_it	1.562	4.5	7728

Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-ID	Dom-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	1	A	1806	tight positional	0.092	0.05
1	1	A	1806	tight thermal	0.192	0.5
1	2	B	1806	tight positional	0.131	0.05
1	2	B	1806	tight thermal	0.228	0.5
1	3	C	1806	tight positional	0.098	0.05
1	3	C	1806	tight thermal	0.189	0.5
1	4	D	1806	tight positional	0.087	0.05
1	4	D	1806	tight thermal	0.19	0.5
1	5	E	1806	tight positional	0.108	0.05
1	5	E	1806	tight thermal	0.216	0.5
1	6	F	1806	tight positional	0.091	0.05
1	6	F	1806	tight thermal	0.182	0.5
1	7	G	1806	tight positional	0.092	0.05
1	7	G	1806	tight thermal	0.193	0.5
2	1	A	647	tight positional	0.072	0.05
2	1	A	647	tight thermal	0.109	0.5
2	2	B	647	tight positional	0.076	0.05
2	2	B	647	tight thermal	0.131	0.5
2	3	C	647	tight positional	0.073	0.05
2	3	C	647	tight thermal	0.105	0.5
2	4	D	647	tight positional	0.07	0.05
2	4	D	647	tight thermal	0.108	0.5
2	5	E	647	tight positional	0.083	0.05
2	5	E	647	tight thermal	0.132	0.5
2	6	F	647	tight positional	0.071	0.05
2	6	F	647	tight thermal	0.102	0.5
2	7	G	647	tight positional	0.076	0.05
2	7	G	647	tight thermal	0.134	0.5
3	1	A	1398	tight positional	0.051	0.05
3	1	A	1398	tight thermal	0.074	0.5
3	2	B	1398	tight positional	0.049	0.05
3	2	B	1398	tight thermal	0.062	0.5
3	3	C	1398	tight positional	0.053	0.05
3	3	C	1398	tight thermal	0.068	0.5
3	4	D	1398	tight positional	0.052	0.05
3	4	D	1398	tight thermal	0.071	0.5
3	5	E	1398	tight positional	0.062	0.05
3	5	E	1398	tight thermal	0.084	0.5
3	6	F	1398	tight positional	0.043	0.05
3	6	F	1398	tight thermal	0.055	0.5
3	7	G	1398	tight positional	0.053	0.05
3	7	G	1398	tight thermal	0.071	0.5

LS refinement shell

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Refine-ID	Num. reflection all
2.7-2.7696	0.368	104	0.327	4270	X-RAY DIFFRACTION	5287
2.77-2.8448	0.345	136	0.295	5988	X-RAY DIFFRACTION	6982
2.845-2.9265	0.305	185	0.284	7102	X-RAY DIFFRACTION	8113
2.927-3.0157	0.297	180	0.263	7032	X-RAY DIFFRACTION	7907
3.016-3.1135	0.275	168	0.246	7055	X-RAY DIFFRACTION	7730
3.114-3.2216	0.291	177	0.231	6979	X-RAY DIFFRACTION	7520
3.222-3.3417	0.252	189	0.22	7037	X-RAY DIFFRACTION	7486
3.342-3.4764	0.273	186	0.223	6976	X-RAY DIFFRACTION	7427
3.476-3.6287	0.236	191	0.213	6994	X-RAY DIFFRACTION	7417
3.629-3.8031	0.25	171	0.207	6983	X-RAY DIFFRACTION	7317
3.803-4.0052	0.22	199	0.197	6673	X-RAY DIFFRACTION	7046
4.005-4.2434	0.234	159	0.184	6519	X-RAY DIFFRACTION	6776
4.243-4.53	0.22	135	0.179	6199	X-RAY DIFFRACTION	6395
4.53-4.8836	0.24	155	0.189	5753	X-RAY DIFFRACTION	5977
4.884-5.3356	0.236	155	0.203	5329	X-RAY DIFFRACTION	5543
5.336-5.942	0.302	136	0.232	4915	X-RAY DIFFRACTION	5098
5.942-6.8168	0.282	117	0.24	4365	X-RAY DIFFRACTION	4527
6.817-8.2431	0.193	87	0.187	3755	X-RAY DIFFRACTION	3866
8.243-11.2409	0.149	84	0.15	3012	X-RAY DIFFRACTION	3109
11.241-30	0.264	52	0.29	1923	X-RAY DIFFRACTION	1983

Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

ID	L11 (°²)	L12 (°²)	L13 (°²)	L22 (°²)	L23 (°²)	L33 (°²)	S11 (Å °)	S12 (Å °)	S13 (Å °)	S21 (Å °)	S22 (Å °)	S23 (Å °)	S31 (Å °)	S32 (Å °)	S33 (Å °)	T11 (Å²)	T12 (Å²)	T13 (Å²)	T22 (Å²)	T23 (Å²)	T33 (Å²)	Origin x (Å)	Origin y (Å)	Origin z (Å)
1	1.7331	-0.5615	0.1677	2.4224	0.0499	1.0618	-0.0692	0.0973	0.0207	-0.0608	0.0442	-0.1251	-0.0603	0.2199	0.025	0.1395	-0.0214	0.0301	0.1502	0.0341	0.0681	1.814	9.025	-16.046
2	0.7464	-0.4006	0.5077	4.3288	2.409	10.4065	-0.0558	0.2315	-0.3382	-0.0892	0.5362	-0.6425	-1.102	1.2376	-0.4804	0.472	0.0428	0.1158	0.6823	0.0152	0.2854	21.146	8.094	-29.449
3	8.3958	-0.8165	-0.2393	8.5617	-0.5763	6.7974	0.3758	-0.0226	-0.6832	-0.3895	-0.635	-0.6171	0.793	1.092	0.2592	0.9534	0.3704	0.0285	0.8082	-0.0347	0.3833	11.128	8.198	-53.402
4	2.742	0.2105	0.3314	1.3934	0.0409	0.6243	-0.03	0.0144	-0.0111	-0.0067	0.0315	0.0637	-0.093	-0.0192	-0.0015	0.1391	-0.0122	-0.0049	0.0915	0.0503	0.0616	-22.272	41.447	-15.065
5	5.3541	-3.5657	-3.2285	5.0155	6.201	8.9604	0.1463	0.0024	0.8154	-0.3071	0.16	-1.0675	-0.1692	0.3375	-0.3062	0.2792	-0.1433	-0.0284	0.3009	0.0489	0.366	-9.509	56.31	-28.196
6	10.5669	0.4592	0.3226	7.5238	-0.3437	6.3543	0.2657	1.3382	0.0652	-0.1697	-0.1015	-0.349	-0.367	1.3108	-0.1641	0.5569	0.0745	0.0073	1.3316	0.1189	0.417	-14.598	47.938	-52.319
7	2.5944	0.4703	-0.1425	2.3196	0.1925	0.928	0.0323	0.0581	0.1732	0.0272	-0.0124	-0.0421	-0.136	-0.0161	-0.0199	0.1188	0.0221	-0.0185	0.1327	0.0559	0.0605	-62.238	42.918	-15.384
8	4.5658	0.6516	-4.0187	-1.3057	1.1108	10.2998	0.6477	0.3729	0.679	-0.5587	-0.4004	-1.0534	-0.4594	-1.0335	-0.2473	0.3958	-0.0674	-0.139	0.3875	0.1321	0.2403	-65.575	62.241	-28.515
9	11.0633	0.6653	0.758	8.4259	0.2803	4.9666	-0.2452	0.4625	-0.0936	-0.1759	0.1082	-0.8788	-0.6678	0.6449	0.137	0.6168	-0.0815	0.0989	0.7694	0.0254	0.5619	-61.721	53.137	-53.043
10	1.8004	-0.1017	-0.1135	3.3481	0.1213	0.6339	0.0364	0.1344	0.0304	0.0462	0.0011	0.237	-0.0191	-0.1455	-0.0375	0.141	-0.0203	-0.0179	0.1525	0.0297	0.0479	-88.466	12.544	-16.135
11	2.2487	2.3861	-2.4507	5.0534	-3.1116	9.4953	0.3501	0.3398	0.8646	0.0145	0.2862	0.3607	0.6153	-1.0063	-0.6363	0.575	0.0826	-0.1212	0.4751	0.0075	0.3116	-105.239	22.323	-29.363
12	8.9987	-1.2501	0.2265	9.4163	0.5263	6.1386	0.182	-0.216	1.3883	-0.6242	-0.2187	0.0693	-1.1584	-0.7403	0.0367	1.1521	0.1274	0.0714	0.5729	0.0099	0.4918	-96.229	19.421	-53.779
13	2.1305	-0.1192	-0.0214	1.7722	-0.1732	0.733	-0.0116	0.0702	0.0376	-0.0843	0.0622	-0.033	0.0343	-0.034	-0.0506	0.1195	-0.0382	-0.0241	0.1026	-0.0085	0.0078	-81.008	-26.959	-17.064
14	1.1355	-1.1067	-0.7138	4.9389	-4.1511	7.5659	-0.2983	0.1491	-0.0376	-0.4186	0.471	0.7386	0.4195	-0.1011	-0.1727	0.1454	-0.0053	-0.0283	0.4252	-0.0135	0.216	-99.023	-33.636	-30.526
15	8.9994	-0.9388	-0.0734	8.1368	0.4886	5.7087	-0.1009	-0.0395	-0.0565	0.1514	0.0307	0.5897	-0.1158	-0.9794	0.0702	0.4935	-0.0014	-0.0599	0.8089	0.068	0.2185	-90.049	-27.807	-54.254
16	3.1087	0.367	-0.0392	2.0373	-0.3131	0.8432	0.0585	0.0136	-0.2883	-0.0942	-0.0335	-0.0117	0.2556	-0.029	-0.025	0.1957	0.0032	-0.018	0.1553	-0.0422	0.1122	-45.577	-45.929	-17.7
17	6.9522	-1.1774	4.7834	5.674	-2.914	8.3163	0.4502	0.3181	-1.5702	0.2448	0.2089	-0.0775	0.7576	0.0601	-0.6591	0.6178	-0.05	-0.0935	0.382	-0.1929	0.6987	-50.935	-64.265	-31.611
18	13.8105	1.0874	-0.3648	8.4567	0.1955	5.9333	-0.537	2.379	-0.042	-0.4613	0.3895	0.545	0.743	-0.9367	0.1474	0.6971	-0.2739	-0.0227	1.5948	-0.0936	0.6169	-49.857	-53.188	-55.401
19	1.659	0.2269	-0.1498	3.1429	-0.0027	1.026	0.033	0.0652	-0.0432	0.0625	-0.0345	-0.0996	0.0976	0.099	0.0015	0.1312	0.0321	0.0144	0.1212	0.0097	0.0367	-8.846	-29.691	-17.378
20	4.4286	1.5271	3.8909	2.8705	-0.3566	10.5975	0.4599	0.4515	-0.8042	0.5204	-0.2493	-0.2854	-0.0145	1.1833	-0.2106	0.5917	0.0317	0.0433	0.4012	-0.0174	0.3196	2.186	-44.95	-31.444
21	8.5195	-0.113	-0.8139	9.072	-0.2258	6.217	-0.1694	-0.3833	-0.254	-0.3782	0.0191	0.6058	0.9342	-0.1226	0.1503	0.7798	-0.0378	-0.0081	0.5555	-0.0055	0.3246	-5.496	-36.69	-55.117

Refinement TLS group

Refine-ID: X-RAY DIFFRACTION / Selection: ALL

ID	Refine TLS-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	A	A	2 - 135	1 - 134
2	1	A	A	410 - 525	409 - 524
3	2	A	A	136 - 190	135 - 189
4	2	A	A	375 - 409	374 - 408
5	3	A	A	191 - 374	190 - 373
6	4	B	B	2 - 135	1 - 134
7	4	B	B	410 - 525	409 - 524
8	5	B	B	136 - 190	135 - 189
9	5	B	B	375 - 409	374 - 408
10	6	B	B	191 - 374	190 - 373
11	7	C	C	2 - 135	1 - 134
12	7	C	C	410 - 525	409 - 524
13	8	C	C	136 - 190	135 - 189
14	8	C	C	375 - 409	374 - 408
15	9	C	C	191 - 374	190 - 373
16	10	D	D	2 - 135	1 - 134
17	10	D	D	410 - 525	409 - 524
18	11	D	D	136 - 190	135 - 189
19	11	D	D	375 - 409	374 - 408
20	12	D	D	191 - 374	190 - 373
21	13	E	E	2 - 135	1 - 134
22	13	E	E	410 - 525	409 - 524
23	14	E	E	136 - 190	135 - 189
24	14	E	E	375 - 409	374 - 408
25	15	E	E	191 - 374	190 - 373
26	16	F	F	2 - 135	1 - 134
27	16	F	F	410 - 525	409 - 524
28	17	F	F	136 - 190	135 - 189
29	17	F	F	375 - 409	374 - 408
30	18	F	F	191 - 374	190 - 373
31	19	G	G	2 - 135	1 - 134
32	19	G	G	410 - 525	409 - 524
33	20	G	G	136 - 190	135 - 189
34	20	G	G	375 - 409	374 - 408
35	21	G	G	191 - 374	190 - 373

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